Tau phosphorylation sites work in concert to promote neurotoxicity in vivo. - Test2 - elhamkhani - TriplyDB

Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

http://www.wikidata.org/entity/Q36173962

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LRRK2 phosphorylates novel tau epitopes and promotes tauopathy Tau-targeted treatment strategies in Alzheimer's disease Lysosomal dysfunction promotes cleavage and neurotoxicity of tau in vivo Tau physiology and pathomechanisms in frontotemporal lobar degeneration Modeling the complex pathology of Alzheimer's disease in Drosophila Tau promotes neurodegeneration via DRP1 mislocalization in vivo Design and synthesis of a library of lead-like 2,4-bisheterocyclic substituted thiophenes as selective Dyrk/Clk inhibitors Animal models for Alzheimer's disease and frontotemporal dementia: a perspective Loss of vesicular dopamine release precedes tauopathy in degenerative dopaminergic neurons in a Drosophila model expressing human tau.Interaction between eye pigment genes and tau-induced neurodegeneration in Drosophila melanogaster Hirano bodies differentially modulate cell death induced by tau and the amyloid precursor protein intracellular domain.High-content siRNA screening of the kinome identifies kinases involved in Alzheimer's disease-related tau hyperphosphorylation.Tau promotes neurodegeneration through global chromatin relaxation.Tau association with synaptic vesicles causes presynaptic dysfunction.The unfolded protein response protects from tau neurotoxicity in vivo.Transgenic Drosophila models of Alzheimer's disease and tauopathies A DNA damage-activated checkpoint kinase phosphorylates tau and enhances tau-induced neurodegeneration.ASIP Outstanding Investigator Award Lecture. New approaches to the pathology and genetics of neurodegeneration The mammalian target of rapamycin at the crossroad between cognitive aging and Alzheimer's disease.Implicating calpain in tau-mediated toxicity in vivo.Drosophila melanogaster in the study of human neurodegeneration.mNos2 deletion and human NOS2 replacement in Alzheimer disease models γ-Aminobutyric acid type A (GABAA) receptor activation modulates tau phosphorylation.Protein tau: prime cause of synaptic and neuronal degeneration in Alzheimer's disease.Drosophila melanogaster as a model organism for Alzheimer's disease.Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration.Combinatorial Tau pseudophosphorylation: markedly different regulatory effects on microtubule assembly and dynamic instability than the sum of the individual parts Blocking Effects of Human Tau on Squid Giant Synapse Transmission and Its Prevention by T-817 MA.Tau aggregation and its interplay with amyloid-β.Screening Dyrk1A inhibitors by MALDI-QqQ mass spectrometry: systematic comparison to established radiometric, luminescence, and LC-UV-MS assays.What we can learn from animal models about cerebral multi-morbidity.The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation.Hyperphosphorylation of intrinsically disordered tau protein induces an amyloidogenic shift in its conformational ensemble.Expression of 1N3R-Tau isoform inhibits cell proliferation by inducing S phase arrest in N2a cells.NMNAT suppresses tau-induced neurodegeneration by promoting clearance of hyperphosphorylated tau oligomers in a Drosophila model of tauopathy.Drosophila models of proteinopathies: the little fly that could.The many faces of tau Drosophila models of tauopathies: what have we learned?Alzheimer's disease models and functional genomics-How many needles are there in the haystack?

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P2860

Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

http://www.wikidata.org/entity/Q36173962

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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name

Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

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Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

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Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

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Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

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Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

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Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

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MBC.E07-04-0327

P1433

Molecular Biology of the Cell

P1476

Tau phosphorylation sites work in concert to promote neurotoxicity in vivo.

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P2093

Daniel L Felch

http://www.w3.org/2001/XMLSchema#string

Dora Dias-Santagata

http://www.w3.org/2001/XMLSchema#string

Mel B Feany

http://www.w3.org/2001/XMLSchema#string

Michelle L Steinhilb

http://www.w3.org/2001/XMLSchema#string

Tudor A Fulga

http://www.w3.org/2001/XMLSchema#string

P2860

Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer's disease

Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation

Neurodegenerative tauopathies

A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis.

Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo

The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region

Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau.

Genetic modifiers of tauopathy in Drosophila.

Post-translational modifications of tau protein in Alzheimer's disease.

Mitotic mechanisms in Alzheimer's disease?

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5060-5068

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scholarly article

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10.1091/MBC.E07-04-0327

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12

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18

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2007-10-10T00:00:00Z

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17928404

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phosphorylation

P932

2096612

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